HXKG_KLULA
ID HXKG_KLULA Reviewed; 481 AA.
AC Q6CUZ3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glucokinase-1;
DE EC=2.7.1.2 {ECO:0000269|PubMed:17573926};
DE AltName: Full=Glucose kinase 1;
DE Short=GLK-1;
DE AltName: Full=Hexokinase GLK1 {ECO:0000305};
DE EC=2.7.1.1 {ECO:0000269|PubMed:17573926};
GN Name=GLK1; OrderedLocusNames=KLLA0C01155g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17573926; DOI=10.1111/j.1567-1364.2007.00259.x;
RA Kettner K., Mueller E.-C., Otto A., Roedel G., Breunig K.D., Kriegel T.M.;
RT "Identification and characterization of a novel glucose-phosphorylating
RT enzyme in Kluyveromyces lactis.";
RL FEMS Yeast Res. 7:683-692(2007).
CC -!- FUNCTION: Glukokinase specific for aldohexoses. Phosphorylates glucose
CC and mannose, but not fructose. {ECO:0000269|PubMed:17573926}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2;
CC Evidence={ECO:0000269|PubMed:17573926};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000269|PubMed:17573926};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:17573926};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000269|PubMed:17573926};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:17573926};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC Evidence={ECO:0000269|PubMed:17573926};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000269|PubMed:17573926}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000269|PubMed:17573926}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; CR382123; CAH01097.1; -; Genomic_DNA.
DR RefSeq; XP_452246.1; XM_452246.1.
DR PDB; 6R2N; X-ray; 2.60 A; A/B/C=2-481.
DR PDBsum; 6R2N; -.
DR AlphaFoldDB; Q6CUZ3; -.
DR SMR; Q6CUZ3; -.
DR STRING; 28985.XP_452246.1; -.
DR PRIDE; Q6CUZ3; -.
DR EnsemblFungi; CAH01097; CAH01097; KLLA0_C01155g.
DR GeneID; 2892353; -.
DR KEGG; kla:KLLA0_C01155g; -.
DR eggNOG; KOG1369; Eukaryota.
DR HOGENOM; CLU_014393_5_0_1; -.
DR InParanoid; Q6CUZ3; -.
DR OMA; VCSIDLH; -.
DR BRENDA; 2.7.1.2; 2825.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; IEA:EnsemblFungi.
DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0019158; F:mannokinase activity; IEA:EnsemblFungi.
DR GO; GO:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR GO; GO:0019660; P:glycolytic fermentation; IEA:EnsemblFungi.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006013; P:mannose metabolic process; IEA:UniProt.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR019807; Hexokinase_BS.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; PTHR19443; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00378; HEXOKINASE_1; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..481
FT /note="Glucokinase-1"
FT /id="PRO_0000364088"
FT DOMAIN 4..477
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 64..204
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 146..172
FT /note="Glucose-binding"
FT /evidence="ECO:0000255"
FT REGION 205..466
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 466..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 21..38
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 79..91
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 117..135
FT /evidence="ECO:0007829|PDB:6R2N"
FT TURN 137..142
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:6R2N"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:6R2N"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 226..245
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6R2N"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:6R2N"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 348..355
FT /evidence="ECO:0007829|PDB:6R2N"
FT TURN 359..363
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 380..412
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 438..448
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 452..456
FT /evidence="ECO:0007829|PDB:6R2N"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:6R2N"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:6R2N"
FT HELIX 470..477
FT /evidence="ECO:0007829|PDB:6R2N"
SQ SEQUENCE 481 AA; 53757 MW; 3894D9AA9FD5BEF5 CRC64;
MSDPKLTKAV DSICDQFIVT KSKISQLTEY FIDCMEKGLE PCESDISQNK GLPMIPTFVT
DKPSGQEHGV TMLAADLGGT NFRVCSVELL GNHEFKIEQE KSKIPTFFFQ DDHHVTSKDL
FQHMALITHQ FLTKHHKDVI QDYKWKMGFT FSYPVDQTSL SSGKLIRWTK GFKIGDTVGQ
DVVQLFQQEL NDIGLSNVHV VALTNDTTGT LLARCYASSD AARAINEPVI GCIFGTGTNG
CYMEKLENIH KLDPASREEL LSQGKTHMCI NTEWGSFDNE LNHLPTTSYD IKIDQQFSTN
PGFHLFEKRV SGLYLGEILR NILLDLEKQE LFDLKESVLK NNPFILTTET LSHIEIDTVE
NDLQDTRDAL LKAADLETTF EERVLIQKLV RAISRRAAFL AAVPIAAILI KTNALNQSYH
CQVEVGCDGS VVEHYPGFRS MMRHALALSP IGPEGERDVH LRISKDGSGV GAALCALHAN
Y
